The amino acid sequence of the heavy chain of an IgA2, AIm(1) polymeric myeloma protein (Avil) was studied. Altogether, sequence data were obtained for some 130 residues. Including the amino acids placed by homology with IgA1, this accounts for some 170 residues, thus representing more than one-third of the alpha2 chain. The sequence includes 26 amino acids from the amino-terminal end (V-H III), and 25 residues at the "hinge" region. Of a total of 17 cysteine residues, 14 were located in regions of the molecule which were identical or homologous in the alpha1 and alpha2 chains. These striking homologies, together with the results obtained by diagonal maps of classes of IgA. Study of the cysteine-containing peptides of the J chain are consistent with the conclusion that the J chains associated with different classes of immunoglobulins are identical.
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